Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

p62/Sequestosome 1 levels increase and phosphorylation is altered in Cx50D47A lenses, but deletion of p62/sequestosome 1 does not improve transparency.

Molecular vision - 1 Jan 2020

Jara Oscar, Mysliwiec Hubert, Minogue Peter J, Berthoud Viviana M, Beyer Eric C

Abstract excerpt

Purpose: p62/Sequestosome 1 (p62) is a stress-induced protein that is involved in several different intracellular pathways, including regulation of aspects of protein degradation. p62 levels are elevated in several types of cataracts. We investigated whether levels of p62 and its phosphorylation were altered in the lenses of Cx50D47A mice, which express a mutant of connexin50 (Cx50) that leads to cataracts and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Autophagy-Related Proteins
Share to Cataract

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Connexins

Share to Histones

Share to Lens, Crystalline

Share to Mitochondrial Precursor Protein Import Complex Proteins

Share to Receptors, Cell Surface

Share to Sequestosome-1 Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 32214786
PMCID: PMC7090271

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

p62/Sequestosome 1 levels increase and phosphorylation is altered in Cx50D47A lenses, but deletion of p62/sequestosome 1 does not improve transparency.PMID 32214786Read ↗

p62 expression and autophagy in αB-crystallin R120G mutant knock-in mouse model of hereditary cataract.Semantic proximity Read ↗

Connexin50D47A Decreases Levels of Fiber Cell Connexins and Impairs Lens Fiber Cell DifferentiationSemantic proximity Read ↗

Cataract-linked serine mutations in the gap junction protein connexin50 expose a sorting signal that promotes its lysosomal degradation.Semantic proximity Read ↗

The unfolded protein response is activated in connexin 50 mutant mouse lenses.Semantic proximity Read ↗

Autophagy and UPR in alpha-crystallin mutant knock-in mouse models of hereditary cataracts.Semantic proximity Read ↗

Connexin46fs380 Causes Progressive CataractsSemantic proximity Read ↗

Identification of proteins that modify cataract of mouse eye lens.Semantic proximity Read ↗

Connexin Mutants Compromise the Lens Circulation and Cause Cataracts through Biomineralization.Semantic proximity Read ↗

A connexin50 mutant, CX50fs, that causes cataracts is unstable, but is rescued by a proteasomal inhibitor.Semantic proximity Read ↗

Defect of mitotic vimentin phosphorylation causes microophthalmia and cataract via aneuploidy and senescence in lens epithelial cells.Semantic proximity Read ↗

Focus on lens connexins.Semantic proximity Read ↗

Activation of the unfolded protein response by a cataract-associated αA-crystallin mutation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.